scholarly journals Induced Self-Assembly and Förster Resonance Energy Transfer Studies of Alkynylplatinum(II) Terpyridine Complex Through Interaction With Water-Soluble Poly(phenylene ethynylene sulfonate) and the Proof-of-Principle Demonstration of this Two-Component Ensemble for Selective Label-Free Detection of Human Serum Albumin

2011 ◽  
Vol 133 (46) ◽  
pp. 18775-18784 ◽  
Author(s):  
Clive Yik-Sham Chung ◽  
Vivian Wing-Wah Yam
Keyword(s):  
Self Assembly ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Water Soluble ◽  
Label Free ◽  
Phenylene Ethynylene ◽  
Label Free Detection ◽  
Two Component ◽  
Selective Label ◽  
Soluble Poly

Programmable in vitro Co-Encapsidation of Guest Proteins Inside Protein Nanocages

2018 ◽  
Author(s):  
Noor H. Dashti ◽  
Rufika S. Abidin ◽  
Frank Sainsbury
Keyword(s):  
Self Assembly ◽  
Mammalian Cells ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Super Resolution ◽  
Cell Engineering ◽  
Particle Analysis ◽  
Protein Cages

Bioinspired self-sorting and self-assembling systems using engineered versions of natural protein cages have been developed for biocatalysis and therapeutic delivery. The packaging and intracellular delivery of guest proteins is of particular interest for both <i>in vitro</i> and <i>in vivo</i> cell engineering. However, there is a lack of platforms in bionanotechnology that combine programmable guest protein encapsidation with efficient intracellular uptake. We report a minimal peptide anchor for <i>in vivo</i> self-sorting of cargo-linked capsomeres of the Murine polyomavirus (MPyV) major coat protein that enables controlled encapsidation of guest proteins by <i>in vitro</i> self-assembly. Using Förster resonance energy transfer (FRET) we demonstrate the flexibility in this system to support co-encapsidation of multiple proteins. Complementing these ensemble measurements with single particle analysis by super-resolution microscopy shows that the stochastic nature of co-encapsidation is an overriding principle. This has implications for the design and deployment of both native and engineered self-sorting encapsulation systems and for the assembly of infectious virions. Taking advantage of the encoded affinity for sialic acids ubiquitously displayed on the surface of mammalian cells, we demonstrate the ability of self-assembled MPyV virus-like particles to mediate efficient delivery of guest proteins to the cytosol of primary human cells. This platform for programmable co-encapsidation and efficient cytosolic delivery of complementary biomolecules therefore has enormous potential in cell engineering.

scholarly journals Comparison of DNAzyme activity for the development of an immobilized heme sensor

MRS Advances ◽  
2018 ◽  
Vol 3 (26) ◽  
pp. 1491-1496
Author(s):  
Natalie Hughes ◽  
Nancy Nguyen ◽  
Deanna-Kaye Daley ◽  
Justin Grennell ◽  
Amira Gee ◽  
...  
Keyword(s):  
Self Assembly ◽  
Point Of Care ◽  
Label Free ◽  
Detection Range ◽  
Chemical Complexity ◽  
Detection Strategy ◽  
Detection Approach ◽  
Label Free Detection ◽  
G Quadruplex ◽  
Care Systems

ABSTRACTPoint-of-care systems require highly sensitive, quantitative and selective detection platforms for the real-time multiplexed monitoring of target analytes. To ensure facile development of a sensor, it is preferable for the detection assay to have minimal chemical complexity, contain no wash steps and provide a wide and easily adaptable detection range for multiple targets. Current studies involve label-free detection strategy for relevant clinical molecules such as heme using G-quadruplex based self-assembly. We have explored the measurement of binding and kinetic parameters of various G-quadruplex/heme complexes which are able to self-associate to form a DNAzyme with peroxidase mimicking capabilities and are critical to nucleic acid research. The detection strategy includes immobilizing the G-quadruplex sequences within a polymer matrix to provide a self-assembly based detection approach for heme that could be translated towards other clinically relevant targets.

scholarly journals Peptide-coated palladium nanoparticle for highly sensitive bioanalysis of trypsin in human urine samples

2018 ◽  
Vol 8 ◽  
pp. 184798041882039 ◽  
Author(s):  
Guohua Zhou ◽  
Huimin Jiang ◽  
Yanfang Zhou ◽  
Peilian Liu ◽  
Yongmei Jia ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Palladium Nanoparticles ◽  
Limit Of Detection ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Water Soluble ◽  
Urine Samples ◽  
Fluorescence Resonance ◽  
Functional Peptide

In recent years, palladium nanoparticles have been proved as energy acceptor candidates in fluorescence resonance energy transfer-based sensors for analytical and biological purposes. In this article, peptide-coated palladium nanoparticles were prepared using a simple one-step preparation method. The peptide Cys-Ala-Leu-Asn-Asn was used as a ligand, whereas hydrazine hydrate was used as a reductant to obtain water-soluble and stable peptide-coated palladium nanoparticles. Additionally, peptide-coated palladium nanoparticles were functionalized by adding the functional peptide CALNNGGARK(FITC) in combination with Cys-Ala-Leu-Asn-Asn during the preparation process. The prepared functionalized peptide-coated palladium nanoparticles were used for trypsin detection based on the fluorescence resonance energy transfer approach. Under optimized conditions, the proposed method can be used for the detection of trypsin concentrations in the range of approximately 0.2–8-μg/mL with a limit of detection of 0.18-μg/mL. The functionalized peptide-coated palladium nanoparticles were successfully applied for the detection of trypsin in urine samples. Our findings also indicated that peptide-coated palladium nanoparticles can highly quench fluorophores and are suitable for the manufacture of off–on state fluorescent sensors. We anticipated that the peptide-coated palladium nanoparticles proposed in this article will have great potential for the detection of trypsin in urine and other analytical, biological, and clinical applications.

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